ID A0A7T5BXY7_ANTFL Unreviewed; 261 AA. AC A0A7T5BXY7; DT 02-JUN-2021, integrated into UniProtKB/TrEMBL. DT 02-JUN-2021, sequence version 1. DT 02-OCT-2024, entry version 10. DE RecName: Full=Cytochrome c oxidase subunit 3 {ECO:0000256|ARBA:ARBA00015944, ECO:0000256|RuleBase:RU003375}; GN Name=COX3 {ECO:0000313|EMBL:QQD89998.1}; OS Antechinus flavipes (Yellow-footed marsupial mouse) (Phascogale flavipes). OG Mitochondrion {ECO:0000313|EMBL:QQD89998.1}. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Metatheria; Dasyuromorphia; Dasyuridae; Antechinus. OX NCBI_TaxID=38775 {ECO:0000313|EMBL:QQD89998.1}; RN [1] {ECO:0000313|EMBL:QQD89998.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Adam Ant {ECO:0000313|EMBL:QQD89998.1}; RA Seim I.; RT "The mitochondrial genome of the yellow-footed dusky antechinus, Antechinus RT flavipes."; RL Submitted (SEP-2019) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Component of the cytochrome c oxidase, the last enzyme in the CC mitochondrial electron transport chain which drives oxidative CC phosphorylation. The respiratory chain contains 3 multisubunit CC complexes succinate dehydrogenase (complex II, CII), ubiquinol- CC cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CC CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to CC transfer electrons derived from NADH and succinate to molecular oxygen, CC creating an electrochemical gradient over the inner membrane that CC drives transmembrane transport and the ATP synthase. Cytochrome c CC oxidase is the component of the respiratory chain that catalyzes the CC reduction of oxygen to water. Electrons originating from reduced CC cytochrome c in the intermembrane space (IMS) are transferred via the CC dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 CC to the active site in subunit 1, a binuclear center (BNC) formed by CC heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 CC water molecules using 4 electrons from cytochrome c in the IMS and 4 CC protons from the mitochondrial matrix. {ECO:0000256|RuleBase:RU003375}. CC -!- CATALYTIC ACTIVITY: CC Reaction=4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)- CC [cytochrome c] + 4 H(+)(out) + 2 H2O; Xref=Rhea:RHEA:11436, CC Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, CC ChEBI:CHEBI:29034; EC=7.1.1.9; CC Evidence={ECO:0000256|ARBA:ARBA00029331}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11437; CC Evidence={ECO:0000256|ARBA:ARBA00029331}; CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi- CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. CC -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 3 family. CC {ECO:0000256|ARBA:ARBA00010581, ECO:0000256|RuleBase:RU003375}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; MN447797; QQD89998.1; -; Genomic_DNA. DR AlphaFoldDB; A0A7T5BXY7; -. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW. DR GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:InterPro. DR GO; GO:0019646; P:aerobic electron transport chain; IEA:InterPro. DR CDD; cd01665; Cyt_c_Oxidase_III; 1. DR Gene3D; 1.10.287.70; -; 1. DR Gene3D; 1.20.120.80; Cytochrome c oxidase, subunit III, four-helix bundle; 1. DR InterPro; IPR024791; Cyt_c/ubiquinol_Oxase_su3. DR InterPro; IPR033945; Cyt_c_oxase_su3_dom. DR InterPro; IPR000298; Cyt_c_oxidase-like_su3. DR InterPro; IPR035973; Cyt_c_oxidase_su3-like_sf. DR InterPro; IPR013833; Cyt_c_oxidase_su3_a-hlx. DR PANTHER; PTHR11403:SF7; CYTOCHROME C OXIDASE SUBUNIT 3; 1. DR PANTHER; PTHR11403; CYTOCHROME C OXIDASE SUBUNIT III; 1. DR Pfam; PF00510; COX3; 1. DR SUPFAM; SSF81452; Cytochrome c oxidase subunit III-like; 1. DR PROSITE; PS50253; COX3; 1. PE 3: Inferred from homology; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius}; KW Mitochondrion {ECO:0000256|RuleBase:RU003375, ECO:0000313|EMBL:QQD89998.1}; KW Translocase {ECO:0000256|ARBA:ARBA00022967}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, KW ECO:0000256|RuleBase:RU003375}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 16..35 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 41..58 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 79..102 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 129..147 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 159..179 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 191..220 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 240..260 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 4..261 FT /note="Heme-copper oxidase subunit III family profile" FT /evidence="ECO:0000259|PROSITE:PS50253" SQ SEQUENCE 261 AA; 29848 MW; 587B9B7AD3F2873B CRC64; MTHQTHAYHM VNPSPWPLTG ALSAFLLTSG MIMWFHFHST LLLFMGVTSI LLTMFQWWRD VVREGTYQGH HTPVVQKGLR YGMVLFIMSE VFFFVGFFWA FYHSSLSPAL ELGGCWPPVG INPLNPLEVP LLNTAILLAS GVSITWAHHS LMEGNRNQMI QALATTIGLG LYFTILQAME YYEAPFTISD GIYGSTFFVA TGFHGLHVII GSLFLIVCLL RQLFYHFTST HHFGFEAAAW YWHFVDVVWL FLYVSIYWWG S //